PMID:21708137
| Citation |
Blencowe, DK, Al Jubori, S and Morby, AP (2011) Identification of a novel function for the FtsL cell division protein from Escherichia coli K12. Biochem. Biophys. Res. Commun. 411:44-9 |
|---|---|
| Abstract |
Analysis of the essential cell division protein FtsL demonstrates the partial conservation of a cysteine-pair within the trans-membrane region which itself is flanked by histidine-pairs in the cytosol and periplasm. Similar arrangements of such amino acids are seen in proteins known to transport/bind metal ions in biological systems. Heterologous expression of ftsL in Escherichia coli K12 confers a Zn(II)-sensitive phenotype and alteration of the candidate metal-ion binding residues cysteine or histidine substantially alters this phenotype. Whilst the cysteine/histidine replacement derivatives of ftsL were able to complement an otherwise ftsL-null strain, the derivative carrying ftsL lacking the cysteine pair was sensitive to raised metal-ion concentrations in the media. We show that ftsL can confer a metal-ion sensitive phenotype and that trans-membrane cysteine residues play a role in FtsL function in elevated metal-ion concentrations. |
| Links |
PubMed Online version:10.1016/j.bbrc.2011.06.083 |
| Keywords |
Amino Acid Sequence; Cell Cycle Proteins/chemistry; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Consensus Sequence; Cysteine/chemistry; Cysteine/genetics; Drug Resistance, Bacterial; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Histidine/chemistry; Histidine/genetics; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Zinc/metabolism; Zinc/pharmacology |
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